Succinylated wheat germ agglutinin (Succ-WGA) is affinity purified from the native wheat germ agglutinin (WGA). It is dimeric at pH as low as 5 and dissociates at pH lower than 4.5. Succ-WGA agglutinates rabbit erythrocytes at a minimal concentration of about 2g/ml, and agglutinates human erythrocytes of blood groups A, B, and O types. The solubility of Succ-WGA is around 100 times higher than the unmodified lectin at neutral pH. Ulike native WGA, Succ-WGA does not bind to sialic acid residues but retains its specificity towards N-acetylglucosamine. The use of conjugates of the native WGA and the succinylated allows to distinguish between sialylated glycoconjugates and others N-acetylglucosamine structures. See other Succ-WGA conjugates.
Alkaline phosphatase (AP) is conjugated to Succinylated Triticum vulgaris Lectin (Succ WGA) to show the binding of Succ WGA in many applications including Western blotting and ELISA. Alkaline phosphatase is a large protein (140 kDa) that catalyzes the hydrolysis of phosphate groups from a substrate resulting in a colored or fluorescent product. The optimal enzymatic activity of this protein is between pH 8 and 10, and its reaction rate remains linear, improving sensitivity over time.